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Conserved domains on  [gi|502978744|ref|WP_013213720|]
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MULTISPECIES: alpha/beta fold hydrolase [Ralstonia solanacearum species complex]

Protein Classification

alpha/beta hydrolase( domain architecture ID 1002777)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
protocat_pcaD super family cl31213
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 18-267 8.18e-81

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


The actual alignment was detected with superfamily member TIGR02427:

Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 244.19  E-value: 8.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   18 RIRYRIDGADG--PWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDALSIAQ 95
Cdd:TIGR02427   1 RLHYRLDGAADgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   96 VHFVGLSMGGMVAQILGVRHPQRLLSLTLCDTVCHtpIAAHPMWDERIGQVEAHGMAGIVEPTLQRWLTTPFREARPEVA 175
Cdd:TIGR02427  81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAK--IGTPESWNARIAAVRAEGLAALADAVLERWFTPGFREAHPARL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  176 ARVRALLLATAPHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAHLAPIEQ 255
Cdd:TIGR02427 159 DLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQ 238

                         250
                  ....*....|..
gi 502978744  256 EEAFLTDLDEFL 267
Cdd:TIGR02427 239 PEAFNAALRDFL 250
 
Name Accession Description Interval E-value
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 18-267 8.18e-81

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 244.19  E-value: 8.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   18 RIRYRIDGADG--PWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDALSIAQ 95
Cdd:TIGR02427   1 RLHYRLDGAADgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   96 VHFVGLSMGGMVAQILGVRHPQRLLSLTLCDTVCHtpIAAHPMWDERIGQVEAHGMAGIVEPTLQRWLTTPFREARPEVA 175
Cdd:TIGR02427  81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAK--IGTPESWNARIAAVRAEGLAALADAVLERWFTPGFREAHPARL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  176 ARVRALLLATAPHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAHLAPIEQ 255
Cdd:TIGR02427 159 DLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQ 238

                         250
                  ....*....|..
gi 502978744  256 EEAFLTDLDEFL 267
Cdd:TIGR02427 239 PEAFNAALRDFL 250
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-270 5.44e-55

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 177.12  E-value: 5.44e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   7 TESGHADANGIRIRYRIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAG 86
Cdd:COG0596    2 STPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  87 LLDALSIAQVHFVGLSMGGMVAQILGVRHPQRLLSLTLCDtvchtpiaahpmwderigqveahgmagiveptlqrwlttp 166
Cdd:COG0596   82 LLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD---------------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 167 frearpEVAARVRALLL--ATAPHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVL 244
Cdd:COG0596  122 ------EVLAALAEPLRrpGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 502978744 245 PRAAHLAPIEQEEAFLTDLDEFLGHA 270
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 29-254 6.50e-28

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 107.59  E-value: 6.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   29 PWIMLAHALGVDHQMWDSIAHRLSR-RHRVLRYDARGHGGTTAPH--GAYTLFQMADDAAGLLDALSIAQVHFVGLSMGG 105
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  106 MVAQILGVRHPQRLLSLTLCDTvcHTPIAAHPMWDERIGQVEAHGMAGIVEPTLQRWL---------TTPFRE----ARP 172
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFDGFVADFAPNPLgrlvakllaLLLLRLrllkALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  173 EVAARVRALLLATA---PHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAH 249
Cdd:pfam00561 159 LLNKRFPSGDYALAkslVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*
gi 502978744  250 LAPIE 254
Cdd:pfam00561 239 FAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 12-270 5.53e-25

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 102.33  E-value: 5.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  12 ADANGIRIRY-RIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDA 90
Cdd:PRK14875 114 ARIGGRTVRYlRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  91 LSIAQVHFVGLSMGGMVAQILGVRHPQRLLSLTLcdtvchtpIAAHPMWDErIGQVEAHGMAGI-----VEPTLQRWLTT 165
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTL--------IAPAGLGPE-INGDYIDGFVAAesrreLKPVLELLFAD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 166 P-----------FREARPE-VAARVRALLLATAPHGyvgaclaIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIA 233
Cdd:PRK14875 265 PalvtrqmvedlLKYKRLDgVDDALRALADALFAGG-------RQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 502978744 234 egiPNARLKVLPRAAHLAPIEQEEAFLTDLDEFLGHA 270
Cdd:PRK14875 338 ---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
 
Name Accession Description Interval E-value
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 18-267 8.18e-81

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 244.19  E-value: 8.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   18 RIRYRIDGADG--PWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDALSIAQ 95
Cdd:TIGR02427   1 RLHYRLDGAADgaPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   96 VHFVGLSMGGMVAQILGVRHPQRLLSLTLCDTVCHtpIAAHPMWDERIGQVEAHGMAGIVEPTLQRWLTTPFREARPEVA 175
Cdd:TIGR02427  81 AVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAAK--IGTPESWNARIAAVRAEGLAALADAVLERWFTPGFREAHPARL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  176 ARVRALLLATAPHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAHLAPIEQ 255
Cdd:TIGR02427 159 DLYRNMLVRQPPDGYAGCCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPCVEQ 238

                         250
                  ....*....|..
gi 502978744  256 EEAFLTDLDEFL 267
Cdd:TIGR02427 239 PEAFNAALRDFL 250
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-270 5.44e-55

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 177.12  E-value: 5.44e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   7 TESGHADANGIRIRYRIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAG 86
Cdd:COG0596    2 STPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  87 LLDALSIAQVHFVGLSMGGMVAQILGVRHPQRLLSLTLCDtvchtpiaahpmwderigqveahgmagiveptlqrwlttp 166
Cdd:COG0596   82 LLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD---------------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 167 frearpEVAARVRALLL--ATAPHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVL 244
Cdd:COG0596  122 ------EVLAALAEPLRrpGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVL 195

                        250       260
                 ....*....|....*....|....*.
gi 502978744 245 PRAAHLAPIEQEEAFLTDLDEFLGHA 270
Cdd:COG0596  196 PGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 29-254 6.50e-28

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 107.59  E-value: 6.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   29 PWIMLAHALGVDHQMWDSIAHRLSR-RHRVLRYDARGHGGTTAPH--GAYTLFQMADDAAGLLDALSIAQVHFVGLSMGG 105
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSSRPKaqDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  106 MVAQILGVRHPQRLLSLTLCDTvcHTPIAAHPMWDERIGQVEAHGMAGIVEPTLQRWL---------TTPFRE----ARP 172
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFDGFVADFAPNPLgrlvakllaLLLLRLrllkALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  173 EVAARVRALLLATA---PHGYVGACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAH 249
Cdd:pfam00561 159 LLNKRFPSGDYALAkslVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGH 238


                  ....*
gi 502978744  250 LAPIE 254
Cdd:pfam00561 239 FAFLE 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 12-270 5.53e-25

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 102.33  E-value: 5.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  12 ADANGIRIRY-RIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDA 90
Cdd:PRK14875 114 ARIGGRTVRYlRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  91 LSIAQVHFVGLSMGGMVAQILGVRHPQRLLSLTLcdtvchtpIAAHPMWDErIGQVEAHGMAGI-----VEPTLQRWLTT 165
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTL--------IAPAGLGPE-INGDYIDGFVAAesrreLKPVLELLFAD 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 166 P-----------FREARPE-VAARVRALLLATAPHGyvgaclaIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIA 233
Cdd:PRK14875 265 PalvtrqmvedlLKYKRLDgVDDALRALADALFAGG-------RQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 502978744 234 egiPNARLKVLPRAAHLAPIEQEEAFLTDLDEFLGHA 270
Cdd:PRK14875 338 ---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
14-267 1.27e-21

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.06  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  14 ANGIRIRYRIDGADG---PWIMLAHALGVDHQMWDSIAHRLSRR-HRVLRYDARGHGGTTAPHGAYTLF-QMADDAAGLL 88
Cdd:COG2267   11 RDGLRLRGRRWRPAGsprGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFdDYVDDLRAAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  89 DALSIA---QVHFVGLSMGGMVAQILGVRHPQRLlsltlcdtvchtpiaahpmwderigqveahgmAGIVeptlqrwLTT 165
Cdd:COG2267   91 DALRARpglPVVLLGHSMGGLIALLYAARYPDRV--------------------------------AGLV-------LLA 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 166 PFREARPEVAARVRALLlataphgyvgaclaikALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGI-PNARLKVL 244
Cdd:COG2267  132 PAYRADPLLGPSARWLR----------------ALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLL 195

                        250       260
                 ....*....|....*....|....
gi 502978744 245 PRAAHLAPIEQE-EAFLTDLDEFL 267
Cdd:COG2267  196 PGARHELLNEPArEEVLAAILAWL 219
PRK05855 PRK05855
SDR family oxidoreductase;
14-100 1.91e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 75.79  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  14 ANGIRIRYRIDG-ADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHG--AYTLFQMADDAAGLLDA 90
Cdd:PRK05855  10 SDGVRLAVYEWGdPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRtaAYTLARLADDFAAVIDA 89

                         90
                 ....*....|.
gi 502978744  91 LSI-AQVHFVG 100
Cdd:PRK05855  90 VSPdRPVHLLA 100
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 25-266 2.62e-13

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 67.92  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   25 GADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHgAYTLFQMADDAAGLLDALSIaqvhFVGLSMG 104
Cdd:TIGR01738   1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFG-PLSLADMAEAIAAQAPDPAI----WLGWSLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  105 GMVAQILGVRHPQRLLSLTlcdTVCHTP-IAAHPMWDERIGQVEAHGMAGIV----EPTLQRWL---TTPFREARPEVAA 176
Cdd:TIGR01738  76 GLVALHIAATHPDRVRALV---TVASSPcFSAREDWPEGIKPDVLTGFQQQLsddyQRTIERFLalqTLGTPTARQDARA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  177 RVRALLLATAPHGYV--GACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAHLAPIE 254
Cdd:TIGR01738 153 LKQTLLARPTPNVQVlqAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLS 232

                         250
                  ....*....|..
gi 502978744  255 QEEAFLTDLDEF 266
Cdd:TIGR01738 233 HAEAFCALLVAF 244
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
31-267 1.33e-10

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 59.96  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  31 IMLAHALGVDHQMWDSIAHRLSRR-HRVLRYDARGHGGTTAPHGAYTLFQMADDAAGLLDALS--IAQVHFVGLSMGGMV 107
Cdd:COG1647   18 VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKagYDKVIVIGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 108 AQILGVRHPQ--RLLSLtlcdtvchtpiaAHPMWDERIGQVEAHgMAGIVEPTLQRWLTTPFREARPEVAARVRALllat 185
Cdd:COG1647   98 ALLLAARYPDvaGLVLL------------SPALKIDDPSAPLLP-LLKYLARSLRGIGSDIEDPEVAEYAYDRTPL---- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 186 aphgyvgacLAIKAL-----DTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGI--PNARLKVLPRAAHLAPIEQE-E 257
Cdd:COG1647  161 ---------RALAELqrlirEVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDSGHVITLDKDrE 231

                        250
                 ....*....|
gi 502978744 258 AFLTDLDEFL 267
Cdd:COG1647  232 EVAEEILDFL 241
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
31-259 1.84e-10

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 60.03  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  31 IMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTApHGAYTLFQMADDAAGLLDALSIaqvhFVGLSMGGMVAQI 110
Cdd:PRK10349  16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRG-FGALSLADMAEAVLQQAPDKAI----WLGWSLGGLVASQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 111 LGVRHPQRLLSLTlcdTVCHTP-IAAHPMW----DERIGQVEAHgMAGIVEPTLQRWL---TTPFREARPEVAARVRALL 182
Cdd:PRK10349  91 IALTHPERVQALV---TVASSPcFSARDEWpgikPDVLAGFQQQ-LSDDFQRTVERFLalqTMGTETARQDARALKKTVL 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502978744 183 LATAPHGYV--GACLAIKALDTRDALLRIACPTLVVVGEDDTGAPVEVARTIAEGIPNARLKVLPRAAHLAPIEQEEAF 259
Cdd:PRK10349 167 ALPMPEVDVlnGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEF 245
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 31-256 9.78e-10

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 57.61  E-value: 9.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   31 IMLAHALGvDHQMW-DSIAHRLSRR-HRVLRYDARGHGGTTAPHGAYTLF-QMADDAAGLLDAlsIAQVH-----FV-GL 101
Cdd:pfam12146   7 VVLVHGLG-EHSGRyAHLADALAAQgFAVYAYDHRGHGRSDGKRGHVPSFdDYVDDLDTFVDK--IREEHpglplFLlGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  102 SMGGMVAQILGVRHPQRLLSLTLCDTVChtpiAAHPMWDERIGQVEAhGMAGIVEPTLQ-------RWLTTpfreaRPEV 174
Cdd:pfam12146  84 SMGGLIAALYALRYPDKVDGLILSAPAL----KIKPYLAPPILKLLA-KLLGKLFPRLRvpnnllpDSLSR-----DPEV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  175 AARVRA--LLL-ATAPHGYVGACLAIKALDTRDALLRIacPTLVVVGEDDTGAPVEVARTIAEGIPNA--RLKVLPRAAH 249
Cdd:pfam12146 154 VAAYAAdpLVHgGISARTLYELLDAGERLLRRAAAITV--PLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLYH 231


                  ....*..
gi 502978744  250 LAPIEQE 256
Cdd:pfam12146 232 ELLNEPD 238
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 31-257 1.86e-09

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 56.33  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   31 IMLAHALGVDHqmwDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTlfQMADDAAGLLDALSIAQVHFVGLSMGGMVAqi 110
Cdd:pfam12697   1 VVLVHGAGLSA---APLAALLAAGVAVLAPDLPGHGSSSPPPLDLA--DLADLAALLDELGAARPVVLVGHSLGGAVA-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  111 lgvrhpQRLLSLTLCDTVCHTPIAAHPMWDERIGQVEAHGMAGIVEPTLQRWLTTPFREARPEVAARVRALLLATAPHGy 190
Cdd:pfam12697  74 ------LAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAAL- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502978744  191 vgacLAIKALDTRDALLRIACPTLVVVGEDDTGAPveVARTIAEGIPNARLKVLPRAAHLAPIEQEE 257
Cdd:pfam12697 147 ----LAALALLPLAAWRDLPVPVLVLAEEDRLVPE--LAQRLLAALAGARLVVLPGAGHLPLDDPEE 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
14-269 3.04e-09

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.18  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  14 ANGIRIRYRI----DGADGPWIMLAHALGVD-HQMWDSIAHRLSRR-HRVLRYDARGHGGTTAPHGaytlFQMADDAAGL 87
Cdd:COG1506    5 ADGTTLPGWLylpaDGKKYPVVVYVHGGPGSrDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWG----GDEVDDVLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  88 LDALS------IAQVHFVGLSMGGMVAQILGVRHPQRllsltlcdtvchtpIAAhpmwderigqveAHGMAGIVEPTLQR 161
Cdd:COG1506   81 IDYLAarpyvdPDRIGIYGHSYGGYMALLAAARHPDR--------------FKA------------AVALAGVSDLRSYY 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 162 WLTTPFREARPEVAARVRALLLATAPHGYVGaclaikaldtrdallRIACPTLVVVGEDDTGAPVEVARTIAEGI----P 237
Cdd:COG1506  135 GTTREYTERLMGGPWEDPEAYAARSPLAYAD---------------KLKTPLLLIHGEADDRVPPEQAERLYEALkkagK 199

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502978744 238 NARLKVLPRAAHLAPIEQEEAFLTDLDEFLGH 269
Cdd:COG1506  200 PVELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
PRK08775 PRK08775
homoserine O-succinyltransferase;
54-271 9.57e-08

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 52.48  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  54 RHRVLRYDARGHGGttAPHGAYTLFQMADDAAGLLDALSIAQVH-FVGLSMGGMVAQILGVRHPQRLLSLtLCDTVCHTp 132
Cdd:PRK08775  99 RFRLLAFDFIGADG--SLDVPIDTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTL-VVVSGAHR- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 133 iaAHPM---W---DERIGQV------EAHGMAGIVEPTLQRWLTTPFREARPEVAARVRALLLATAPHGYVGACLAIKAL 200
Cdd:PRK08775 175 --AHPYaaaWralQRRAVALgqlqcaEKHGLALARQLAMLSYRTPEEFEERFDAPPEVINGRVRVAAEDYLDAAGAQYVA 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744 201 DTR-DALLR--------------IACPTLVVVGEDDTGAPVEVARTIAEGI-PNARLKVLPRA-AHLAPIEQEEAFLTDL 263
Cdd:PRK08775 253 RTPvNAYLRlsesidlhrvdpeaIRVPTVVVAVEGDRLVPLADLVELAEGLgPRGSLRVLRSPyGHDAFLKETDRIDAIL 332


                 ....*...
gi 502978744 264 DEFLGHAG 271
Cdd:PRK08775 333 TTALRSTG 340
PRK10673 PRK10673
esterase;
31-126 2.73e-06

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 47.42  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  31 IMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHG-GTTAPHGAYTlfQMADDAAGLLDALSIAQVHFVGLSMGGMVAQ 109
Cdd:PRK10673  19 IVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGlSPRDPVMNYP--AMAQDLLDTLDALQIEKATFIGHSMGGKAVM 96

                         90
                 ....*....|....*..
gi 502978744 110 ILGVRHPQRLLSLTLCD 126
Cdd:PRK10673  97 ALTALAPDRIDKLVAID 113
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 31-108 2.90e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 39.43  E-value: 2.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502978744  31 IMLAHALGVDHQMWDSIAHRLSRR-HRVLRYDARGHGGTTAPHGAytlfQMADDAAGLLDALSIAQVHFVGLSMGGMVA 108
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDSAE----QLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 16-71 2.43e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 38.57  E-value: 2.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502978744  16 GIRIRYRIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAP 71
Cdd:PLN02824  17 GYNIRYQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKP 72
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 3-141 7.10e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 37.28  E-value: 7.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744   3 ADAITESGHADANGIRIRYrIDGADGPWIMLAHALGVDHQMWDSIAHRLSRRHRVLRYDARGHGGTTAPHGAYTLFQMAD 82
Cdd:PRK03592   3 VEPPGEMRRVEVLGSRMAY-IETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDYTFADHAR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502978744  83 DAAGLLDALSIAQVHFVGLSMGGMVAQILGVRHPQRLLSLTLCDTVchtpiaAHPM-WDE 141
Cdd:PRK03592  82 YLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAI------VRPMtWDD 135
metX PRK00175
homoserine O-acetyltransferase; Provisional
 80-136 8.06e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 37.48  E-value: 8.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502978744  80 MADDAAGLLDALSIAQVHFV-GLSMGGMVAQILGVRHPQRLLS-LTLCDTVCHTP--IAAH 136
Cdd:PRK00175 132 WVRAQARLLDALGITRLAAVvGGSMGGMQALEWAIDYPDRVRSaLVIASSARLSAqnIAFN 192
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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